ExplorEnz: EC 3.13.2.4

Your query returned 1 entry. Printable version

3.13.2.4

Accepted name:

lanthipeptide synthase

Reaction:

(1) a [protein]-L-serine + a [protein]-L-cysteine = a [protein] with lanthionine crosslink + H₂O (overall reaction)
(1a) a [protein]-L-serine = a [protein]-2-aminoprop-2-enoate + H₂O
(1b) a [protein]-2-aminoprop-2-enoate + a [protein]-L-cysteine = a [protein] with lanthionine crosslink
(2) a [protein]-L-threonine + a [protein]-L-cysteine = a [protein] with 3-methyllanthionine crosslink + H₂O (overall reaction)
(2a) a [protein]-L-threonine = a [protein]-(Z)-2-aminobutenoate + H₂O
(2b) a [protein]-(Z)-2-aminobutenoate + a [protein]-L-cysteine = a [protein] with 3-methyllanthionine crosslink

Other name(s):

lanthipeptide synthetase

Systematic name:

[protein]-(methyl)lanthionine hydrolase

Comments:

The lanthipeptides are a family of ribosomally synthesized and post-translationally modified peptides (RiPPs) that is characterized by the presence of multiple lanthionine (Lan) and 3-methyllanthionine (MeLan) crosslinks, which are formed by lanthipeptide synthases. These enzymes catalyse dehydration of Ser/Thr residues, followed by intramolecular addition of the thiol group of a Cys residue to the dehydro amino acids, which results in the formation of the thioether crosslinks of (methyl)lanthionine.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Li, B., Yu, J.P., Brunzelle, J.S., Moll, G.N., van der Donk, W.A. and Nair, S.K. Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis. Science 311 (2006) 1464–1467. [DOI] [PMID: 16527981]
2.	Willey, J.M. and van der Donk, W.A. Lantibiotics: peptides of diverse structure and function. Annu. Rev. Microbiol. 61 (2007) 477–501. [DOI] [PMID: 17506681]
3.	Li, B. and van der Donk, W.A. Identification of essential catalytic residues of the cyclase NisC involved in the biosynthesis of nisin. J. Biol. Chem. 282 (2007) 21169–21175. [DOI] [PMID: 17513866]
4.	Goto, Y., Li, B., Claesen, J., Shi, Y., Bibb, M.J. and van der Donk, W.A. Discovery of unique lanthionine synthetases reveals new mechanistic and evolutionary insights. PLoS Biol. 8:e1000339 (2010). [DOI] [PMID: 20351769]
5.	Zhang, Q., Yu, Y., Velasquez, J.E. and van der Donk, W.A. Evolution of lanthipeptide synthetases. Proc. Natl. Acad. Sci. USA 109 (2012) 18361–18366. [DOI] [PMID: 23071302]

[EC 3.13.2.4 created 2024]